Background: Plants of the genus Parietaria, Urticaceae family, represent a major cause of pollinosis in the Mediterranean area. Different Parietaria species crossreact to a great extent, but studies on the crossreactivity among the major allergens of these pollens have not been carried out so far.
Objective: To develop an immunochemical method to quantify the major Parietaria judaica allergen, Par j 1, as well as to verify the presence of Par j 1-like proteins in different Urticaceae pollens. These proteins would be purified in order to study the cross-reactivity among them.
Methods: Immunoaffinity chromatography with a monoclonal antibody, solid-phase enzyme-linked immunoassays and SDS-PAGE.
Results: A monoclonal antibody-based ELISA for the quantification of Par j 1 has been developed. The assay has a sensitivity of 0.2 ng/mL and shows a high correlation with the allergenic activity of P. judaica extracts determined by radioallergosorbent assay (RAST) inhibition. By means of this assay, proteins homologous to Par j 1 were detected in P. officinalis and P. mauritanica. These proteins (Par o 1 and Par m 1, respectively) were purified by affinity chromatography using the same monoclonal antibody employed in the ELISA. Crossed-inhibition experiments demonstrated that Par j 1, Par o 1, and Par m 1, competed for the binding of specific IgE from a P. judaica-sensitive patients serum pool.
Conclusion: The results here described suggest that shared allergenic epitopes are present in the three main allergens investigated, which may simplify the diagnosis and therapy for Parietaria allergy.